ID   RBL1B_METPP             Reviewed;         485 AA.
AC   A2SJJ7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain 2 {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Name=cbbL2 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   OrderedLocusNames=Mpe_A2782;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition at
CC       the same active site. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC         bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC         2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC         ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC       chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC       this homodimer is arranged in a barrel-like tetramer with the small
CC       subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM95736.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000555; ABM95736.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A2SJJ7; -.
DR   SMR; A2SJJ7; -.
DR   STRING; 420662.Mpe_A2782; -.
DR   KEGG; mpt:Mpe_A2782; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_2_0_4; -.
DR   Proteomes; UP000000366; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd08212; RuBisCO_large_I; 1.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR   HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   InterPro; IPR020888; RuBisCO_lsuI.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDG01052; RuBisCO; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Photosynthesis; Reference proteome.
FT   CHAIN           1..485
FT                   /note="Ribulose bisphosphate carboxylase large chain 2"
FT                   /id="PRO_0000299965"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        295
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         206
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            335
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         203
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
SQ   SEQUENCE   485 AA;  53310 MW;  3B36C71F79F2FCAD CRC64;
     MNEPTQITDT KKRYAAGVLK YAQMGYWNGD YVPKDTDILA LFRITPQDGV DPIEAAAAVA
     GESSTATWTV VWTDRLTACD MYRAKAYKVE PVPNNPGQYF CYVAYDLSLF EEGSIANVTA
     SIIGNVFSFK PLKAARLEDM KFPVSYVKTF AGPPTGIVVE RERLDKFGRP LLGATTKPKL
     GLSGRNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LFVMDAVNKA SAATGEVKGS
     YLNVTAGTME EMYRRAEFAK ELGSVIIMID LVVGYTAIQS MSNWARQNDM VLHMHRAGHG
     TYTRQKNHGV SFRVIAKWLR MAGVDHLHTG TAVGKLEGDP LTVQGYYNVC RDTHTKVDLP
     RGIFFDQDWG ALKKVMPVAS GGIHAGQMHQ LIDLFGDDVV LQFGGGTIGH PQGIQAGATA
     NRVALEAMVL ARNEGRDIKN EGPQILRDAA KSCTPLAAAL DTWGDITFNY TSTDTSDYVP
     TPSVA
//